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Volumn 12, Issue 5, 2003, Pages 893-902

Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing

Author keywords

AAA+ ATPase; ATP dependent proteolysis; Catalyzed protein unfolding; MantADP; Motor proteins

Indexed keywords

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPX; GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN SSRA; NUCLEOTIDE; PHOSPHOROTHIOIC ACID; PROTEIN; PROTEIN ARC IV37 SSRA; PROTEIN ARC PL8 SSRA; PROTEIN SSRA; UNCLASSIFIED DRUG;

EID: 0037407940     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0237603     Document Type: Article
Times cited : (50)

References (36)
  • 1
    • 0034840284 scopus 로고    scopus 로고
    • ClpX-mediated remodeling of Mu transpososomes: Selective unfolding of subunits destabilizes the entire complex
    • Burton, B.M., Williams, T.L., and Baker, T.A. 2001. ClpX-mediated remodeling of Mu transpososomes: Selective unfolding of subunits destabilizes the entire complex. Mol. Cell 8: 449-454.
    • (2001) Mol. Cell , vol.8 , pp. 449-454
    • Burton, B.M.1    Williams, T.L.2    Baker, T.A.3
  • 2
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • Burton, R.E., Siddiqui, S.M., Kim, Y.-I., Baker, T.A., and Sauer, R.T. 2001. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20: 3092-3100.
    • (2001) EMBO J. , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.-I.3    Baker, T.A.4    Sauer, R.T.5
  • 3
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway, R.C., Brower, C.S., and Conaway, J.W. 2002. Emerging roles of ubiquitin in transcription regulation. Science 296: 1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 4
    • 0017287188 scopus 로고
    • Synthesis and properties of diastereomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate)
    • Eckstein, F. and Goody, R.S. 1976. Synthesis and properties of diastereomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate). Biochemistry 15: 1685-1691.
    • (1976) Biochemistry , vol.15 , pp. 1685-1691
    • Eckstein, F.1    Goody, R.S.2
  • 5
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the ssrA-tagging system
    • Gottesman, S., Roche, E., Zhou, Y., and Sauer, R.T. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the ssrA-tagging system. Genes & Dev. 12: 1338-1347.
    • (1998) Genes & Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 6
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud, R., Kessel, M., Beuron, F., Steven, A.C., and Maurizi, M.R. 1998. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273: 12476-12481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 7
    • 0032189273 scopus 로고    scopus 로고
    • An essential protease involved in bacterial cell-cycle control
    • Jenal, U. and Fuchs, T. 1998. An essential protease involved in bacterial cell-cycle control. EMBO J. 17: 5658-5669.
    • (1998) EMBO J. , vol.17 , pp. 5658-5669
    • Jenal, U.1    Fuchs, T.2
  • 8
    • 0024358181 scopus 로고
    • Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes
    • Jencks, W.P. 1989. Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes. Methods Enzymol. 171: 145-164.
    • (1989) Methods Enzymol. , vol.171 , pp. 145-164
    • Jencks, W.P.1
  • 9
    • 0034046020 scopus 로고    scopus 로고
    • The ssrA-smpB system for protein tagging, directed degradation and ribosome rescue
    • Karzai, A.W., Roche, E.D., and Sauer, R.T. 2000. The ssrA-smpB system for protein tagging, directed degradation and ribosome rescue. Nat. Struct. Bio. 7: 449-455.
    • (2000) Nat. Struct. Bio. , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 10
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim, Y.-I., Burton, R.E., Burton, B.M., Sauer, R.T., and Baker, T.A. 2000. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5: 639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.-I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 12
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis, R., Welty, D.J., and Nakai, H. 1996. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15: 935-944.
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 13
    • 0030048167 scopus 로고    scopus 로고
    • Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp protease
    • Laachouch, J.E., Desmet, L., Geuskens, V., Grimaud, R., and Toussaint, A. 1996. Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp protease. EMBO J. 15: 437-444.
    • (1996) EMBO J. , vol.15 , pp. 437-444
    • Laachouch, J.E.1    Desmet, L.2    Geuskens, V.3    Grimaud, R.4    Toussaint, A.5
  • 14
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M., and Matouschek, A. 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7: 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 15
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L., and Baker, T. 1995. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes & Dev. 9: 2399-2408.
    • (1995) Genes & Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.3
  • 16
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko, I., Smith, C.K., Walsh, N.P., Sauer, R.T., and Baker, T.A. 1997. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91: 939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 17
    • 0037053443 scopus 로고    scopus 로고
    • Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity
    • Li, J. and Sha, B. 2002. Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity. J. Mol. Biol. 318: 1127-1137.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1127-1137
    • Li, J.1    Sha, B.2
  • 18
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylicz, M. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. 88: 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 19
    • 0033866677 scopus 로고    scopus 로고
    • The ClpX protein of Bacillus subtilis indirectly influences RNA polymerase holoenzyme composition and directly stimulates σ-dependent transcription
    • Liu, J. and Zuber, P. 2000. The ClpX protein of Bacillus subtilis indirectly influences RNA polymerase holoenzyme composition and directly stimulates σ-dependent transcription. Mol. Micro. 37: 885-897.
    • (2000) Mol. Micro. , vol.37 , pp. 885-897
    • Liu, J.1    Zuber, P.2
  • 20
    • 0242701440 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M.E., Brown, B.M., Waldbuger, C.D., and Sauer, R.T. 1995. P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemisty 39: 12494-12502.
    • (1995) Biochemisty , vol.39 , pp. 12494-12502
    • Milla, M.E.1    Brown, B.M.2    Waldbuger, C.D.3    Sauer, R.T.4
  • 21
    • 0023809599 scopus 로고
    • Coupled assay of Na+,K+-ATPase activity
    • Norby, J.G. 1988. Coupled assay of Na+,K+-ATPase activity. Methods Enzymol. 156: 116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Norby, J.G.1
  • 22
    • 0034915764 scopus 로고    scopus 로고
    • Mechanism underlying ubiquitination
    • Pickart, C.M. 2001. Mechanism underlying ubiquitination. Annu. Rev. Biochem. 70: 503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 24
    • 0028952291 scopus 로고
    • Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8
    • Schildbach, J.F., Milla, M.E., Jeffrey, P.D., Raumann, B.E., and Sauer, R.T. 1995. Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8. Biochemistry 34: 1405-1412.
    • (1995) Biochemistry , vol.34 , pp. 1405-1412
    • Schildbach, J.F.1    Milla, M.E.2    Jeffrey, P.D.3    Raumann, B.E.4    Sauer, R.T.5
  • 25
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease
    • Singh, S.K., Guo, F., and Maurizi, M.R. 1999. ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry 38: 14906-14915.
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.2    Maurizi, M.R.3
  • 26
    • 0034254908 scopus 로고    scopus 로고
    • Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP
    • Singh, S.K., Grimaud, R., Hoskins, J.R., Wickner, S., and Maurizi, M.R. 2000. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. 97: 8898-8903.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8898-8903
    • Singh, S.K.1    Grimaud, R.2    Hoskins, J.R.3    Wickner, S.4    Maurizi, M.R.5
  • 27
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J.A. 1994. How molecular motors work. Nature 372: 515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 28
    • 0032569898 scopus 로고    scopus 로고
    • Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps
    • Suzuki, Y., Yasunaga, T., Ohkura, R., Wakabayashi, T., and Sutoh, K. 1998. Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps. Nature 396: 380-383.
    • (1998) Nature , vol.396 , pp. 380-383
    • Suzuki, Y.1    Yasunaga, T.2    Ohkura, R.3    Wakabayashi, T.4    Sutoh, K.5
  • 29
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • Thompson, M.W. and Maurizi, M.R. 1994. Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. J. Biol. Chem. 269: 18201-18208.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18201-18208
    • Thompson, M.W.1    Maurizi, M.R.2
  • 30
    • 0029880341 scopus 로고    scopus 로고
    • Evaluation of HIV-1 reverse transcriptase primer tRNA binding by fluorescence spectroscopy: Specificity and comparison to primer/template binding
    • Thrall, S.H., Reinstein, J., Wöhrl, B.M., and Goody, R.S. 1996. Evaluation of HIV-1 reverse transcriptase primer tRNA binding by fluorescence spectroscopy: Specificity and comparison to primer/template binding. Biochemistry 35: 4609-4618.
    • (1996) Biochemistry , vol.35 , pp. 4609-4618
    • Thrall, S.H.1    Reinstein, J.2    Wöhrl, B.M.3    Goody, R.S.4
  • 31
    • 0027250447 scopus 로고
    • Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
    • Todd, M.J., Viitanen, P.V., and Lorimer, G.H. 1993. Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion. Biochemistry 32: 8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 32
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of sspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah, D.A., Levchenko, I., Baker, T.A., and Sauer, R.T. 2002. Characterization of a specificity factor for an AAA+ ATPase: Assembly of sspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9: 1237-1245.
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 33
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang, J., Hartling, J.A., and Flanagan, J.M. 1997. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91: 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 35
    • 0030582703 scopus 로고    scopus 로고
    • Poly-L-lysine activates both peptide and ATP hydrolysis by the ATP-dependent HsIUV protease in Escherichia coli
    • Yoo, S.J., Seol, J.H., Kang, M.-S., and Chung, C.H. 1996. Poly-L-lysine activates both peptide and ATP hydrolysis by the ATP-dependent HsIUV protease in Escherichia coli. Biochem. Biophys. Res. Comm. 229: 531-535.
    • (1996) Biochem. Biophys. Res. Comm. , vol.229 , pp. 531-535
    • Yoo, S.J.1    Seol, J.H.2    Kang, M.-S.3    Chung, C.H.4
  • 36
    • 0035281566 scopus 로고    scopus 로고
    • The RssB response regulator directly targets sS for degradation by ClpXP
    • Zhou, Y., Gottesman, S., Hoskins, J.R., Maurizi, M.R., and Wickner, S. 2001. The RssB response regulator directly targets sS for degradation by ClpXP. Genes & Dev. 15: 627-637.
    • (2001) Genes & Dev. , vol.15 , pp. 627-637
    • Zhou, Y.1    Gottesman, S.2    Hoskins, J.R.3    Maurizi, M.R.4    Wickner, S.5


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